Abstract
Abstract A particulate d-alanine carboxypeptidase present in Bacillus subtilis has been studied. This enzyme has a pH optimum near 5, and is activated by Zn+2 cations. The enzyme is inactivated by penicillin G and activity cannot be restored by washing or by treating it with penicillinase. 14C-Penicillin G is also bound to this particulate enzyme. Both the binding of penicillin G and the inactivation of the carboxypeptidase by penicillin G are reversed by treatment with neutral hydroxylamine, and the kinetics of these two processes is identical. d-Alanine carboxypeptidase activity is also inhibited by sulfhydryl reagents such as iodoacetate in a manner similar to their inhibition of penicillin binding. The possibility that the particulate d-alanine carboxypeptidase may be an uncoupled transpeptidase is discussed.
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